text:
20 Duquesa Fairways
from £40 /night help Price for guests, Nights
8 reviews
from £40 /night help Price for guests, Nights
Estimated nightly price based on a weekly stay. Excludes fees (if applicable). Enter your dates to see the total cost.
Apartment / 3 bedrooms / sleeps 6 Home 148442
Availability Your dates are available
Apartment / 3 bedrooms / sleeps 6
|Key Info
NEW FOR 2015 - High Speed Wi-fi Internet available!
Our beautiful fully air conditioned apartment has 3 bedrooms, 2 bathrooms and 3 Terraces all with fantastic views. It is a real home from home, luxuriously furnished and exceptionally well equipped to ensure you don't need to bring the kitchen sink with you.
Our apartment is ideally equipped for family stays, and having 3 large bedrooms and plenty of outdoor space means it is ideal for larger parties. The all important Wi-fi is an essential for families with older children, (and those of us who simply can't live without it!)
Duquesa Fairways is situated near the top of Monte Duquesa, it has great views over the La Duquesa Golf Course, the mediterranean and beyond to Estepona and Marbella. It is a short walk into the beautiful Puerto de la Duquesa with its excellent supply of shops, bars and restaurants, and of course, the surrounding beaches and beach bars.
|Sleeps up to 6, 3 bedrooms
|3 bedrooms, 2 bathrooms of which 1 Family bathrooms and 1 En suites
|Nearest beach
|Duquesa and Sabinillas 1.5 km
|Will consider
|Corporate bookings, House swap, Long term lets (over 1 month)
|Car advised
|Nearest travel links
|Nearest airport: Malaga 95 km
|Family friendly
|Great for children of all ages
|No pets allowed, No smoking at this property
Features and Facilities
|Log fire, Internet access, DVD player, Sea view
|Shared outdoor pool (unheated), Children's pool
|Central heating, Air conditioning, TV, CD player, Safe, Satellite TV, Wi-Fi available
|Kettle, Toaster, Iron
|Clothes dryer, Dishwasher, Cooker, Microwave, Fridge, Freezer, Washing machine
|Double beds (2), Single beds (2), Cots (1), Dining seats for 6, Lounge seats for 6
|Linen provided, Towels provided, High chair
|Shared outdoor pool (unheated), Balcony or terrace, Shared garden, Swing set
|Secure parking, Lift access, Suitable for people with restricted mobility, Not suitable for wheelchair users
|Further details indoors
Living and Dining area
The living area has 3 seater sofa, wing back chair and footstool. It is equipped with a flat screen TV, DVD, CD Stereo with Aux input to attach your iPod. There is also a good selection of books and DVDs.
The dining area has a 6 seater table (expandable to take 10 but you'll have to bring your own chairs!). There is also a fireplace between the living and dining areas for those of you going in winter.
The Kitchen is fully equipped with everything you will need for a fabulous holiday, including: Dishwasher, Washing Machine, Fridge Freezer, Microwave, Hob & Oven, Kettle, Hand held blender and Toaster as well as all the usual cutlery, crockery, pans, utensils and of course, the all important corkscrew and bottle opener!
As well as air conditioning, all bedrooms have ceiling fans.
The main bedroom has a Super king size bed, ample wardrobe space and an en-suite shower room.
The second bedroom has a standard double bed and a triple wardrobe for storage. It also has access to the front balcony through double sliding patio doors.
Bedroom 3 has 2 singles and is ideal for the kids. It also has a triple wardrobe.
The main terrace is sheltered by a blind on one side to ensure this remains a great place for breakfast or dinner. There is also an outdoor grill for the all important barbeque! Being situated on the corner of a block, it is private, with views down the golf course and to the Mediterranean beyond.
The side terrace is smaller and more suited to a pre-dinner glass of wine or G & T. Put your shades on and watch the sun go down!
The front terrace was built for sun worshippers. It is bathed in sunlight for the majority of the day. Only for the brave!
|Further details outdoors
The beautiful landscaped gardens are not like your average Costa del Sol complex. With heavily planted beds, shady benches, an abundance of fruit trees (you can pick your own lemons and bananas in season) and plenty of space for the kids to run and play around. There is also a swing, slide and paddling pool for the very little ones conveniently situated in the middle of the complex.
Swimming Pools
There are 2 large pools in the complex, with one more than 25 metres long if you fancy a 'real' early morning swim. Both are well stocked with Sun umbrellas and loungers, and there are toilets and shower facilities.
The Andalucia region
If you think you know what to expect from the Costa del Sol, think again! Whilst we still have the miles of golden sandy beaches and beautiful weather, this part of the Costa Del Sol is often referred to as 'the other' Costa Del Sol, because is it so much quieter and less developed than areas closer to Malaga.
Also, you're looking for more than a classic beach/pool or golfing holiday, we are situated within easy driving of some of the most beautiful towns and countryside in Andalucia. Not to mention Gibraltar, or even Africa. If you want to, you really can have a different holiday every day (Or you could just lie by one of our beautifully landscaped pools, and chill!)
Puerto de la Duquesa
A short walk down the hill from our apartment, Duquesa is a beautiful port with many restaurants, bars, clubs and shops. There is ample parking available all around the port, as well as a taxi rank.
As you head back up Monte Duquesa towards the apartment, there is a lovely courtyard with some great bars, restaurants and useful shops.
The small seaside town of Sabinillas sits alongside Duquesa, and still has much of its original charm including houses on the seafront which sell ice creams directly from their windows! There is a further range of excellent restaurants and bars along the beachfront, and the promenade really buzzes in the evening in the summer.
For those of you with younger kids, there are excellent play parks all the way along the sea front between Castillo la Duquesa and Sabinillas, as well as lots of play facilities built directly onto the sand. There are also regular toilet and shower points which make the transition from beach to bar much easier!
Locally, as well as the idyllic beaches, bars and restaurants, there is lots to see. In particular we recommend 'Castillo' (see below), and also the Roman Baths - about 4km inland. These just have to be seen to be believed - very much still in use, we challenge anyone to take a dip inside and not feel the spirits from way back when!
Castillo de la Duquesa
The area just to the west of Duquesa is Castillo de la Duquesa. This is a small 'town' with a number of excellent restaurants and beach bars. It's defence castle is open for a walk around, and well worth a visit.
The beaches here are wide, long and sandy. The surf can get quite high, so we recommend the corner beaches around the port for younger kids. These are much calmer and shallower, and ideal for snorkelling or just lounging around on lilos. All areas are well served by beach bars, where you can also hire loungers and beach umbrellas for the day.
If you want something a bit more adventurous, travel a few km towards Gibraltar and check out the spectacular rocky coves and beaches nestled down below the curving coast road. (some are only accessible by swimming). Here you can snorkel and rock dive in crystal waters to your hearts content.
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19 Aug 2014
"Well appointed , great views in a brilliant position"
We were really looking forward to a sunshine fix , lazing by the pool with a bit of sightseeing thrown in and really enjoyed staying in this lovely apartment. Breakfast on the balcony overlooking the mountains , sea and golf course can't be beaten , and it was so tranquil in the gardens by the pool. The apartment has everything you could wish for and is very modern and clean . With so many places to strike out the week flew by and we will definitely be booking again. Thank you so much !!
19 Aug 2014
"Home from home in the hills!"
Loved this apartment and would definitely return. Everything was beautifully laid out and the apartment is very well equipped with everything you need. There are three fab balconies so you can chase the sun all day and eat outside whilst admiring the views of the mountains and the sea. There are lots of tips on where to go and eat from the owners and other visitors and it's great to walk down the hill into Duquesa for dinner at the marina and a few glasses of the local wine. The owners were quick to respond to our questions prior to the visit and the apartment is easy to find. Great to have car parking too and a pool in beautifully landscaped gardens. Loved it!
12 Jan 2014
"Fantastic Holiday Apartment"
This is my third stay at 20 Duquesa fairways and I can honestly say that this is a real home from home. Beautiful pool, very relaxing! Can't beat watching the sun go down over the mountains and sea on the terrace with a beer. Apartment is very clean and very well stocked with the essentials. Loved having the outdoor grill for dinner. Easy walk to the port which is beautiful during the day and loads of amazing restaurants at night. I expect I'll be back soon!
27 Jul 2013
"great stay in fully equiped appartment with nice pools and great gardens"
I can surely recommend you to stay in this appartement. It was big enough to stay with six people. The balcony is a good place when it is too hot in the sun. In the town Portue de desque you can eat well for a small budget. I especially enjoyed the pools this summer.
4 Nov 2011
"Wonderful Holiday Apartment"
We had a lovely week holiday - the apartment is everything stated, it was also lovely and clean. The grey folder available holds an abundance of information so grab a drink and take the time to look through. Apartment highly reccomended
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Page 1
BioMed Central
Page 1 of 10
(page number not for citation purposes)
BMC Genomics
Open Access
Research article
Evolution from a respiratory ancestor to fill syntrophic and
fermentative niches: comparative fenomics of six Geobacteraceae
Jessica E Butler*, Nelson D Young and Derek R Lovley
Address: Department of Microbiology, 203 Morrill Science Center IVN, University of Massachusetts, 639 North Pleasant Street, Amherst, MA
Email: Jessica E Butler* - email@example.com; Nelson D Young - email@example.com;
Derek R Lovley - firstname.lastname@example.com
* Corresponding author
Background: The anaerobic degradation of organic matter in natural environments, and the
biotechnical use of anaerobes in energy production and remediation of subsurface environments,
both require the cooperative activity of a diversity of microorganisms in different metabolic niches.
The Geobacteraceae family contains members with three important anaerobic metabolisms:
fermentation, syntrophic degradation of fermentation intermediates, and anaerobic respiration.
Results: In order to learn more about the evolution of anaerobic microbial communities, the
genome sequences of six Geobacteraceae species were analyzed. The results indicate that the last
common Geobacteraceae ancestor contained sufficient genes for anaerobic respiration, completely
oxidizing organic compounds with the reduction of external electron acceptors, features that are
still retained in modern Geobacter and Desulfuromonas species. Evolution of specialization for
fermentative growth arose twice, via distinct lateral gene transfer events, in Pelobacter carbinolicus
and Pelobacter propionicus. Furthermore, P. carbinolicus gained hydrogenase genes and genes for
ferredoxin reduction that appear to permit syntrophic growth via hydrogen production. The gain
of new physiological capabilities in the Pelobacter species were accompanied by the loss of several
key genes necessary for the complete oxidation of organic compounds and the genes for the c-type
cytochromes required for extracellular electron transfer.
Conclusion: The results suggest that Pelobacter species evolved parallel strategies to enhance their
ability to compete in environments in which electron acceptors for anaerobic respiration were
limiting. More generally, these results demonstrate how relatively few gene changes can
dramatically transform metabolic capabilities and expand the range of environments in which
microorganisms can compete.
The global carbon cycle and the production of a number
of biofuels depends on the cooperative interaction of a
physiological diversity of anaerobic microorganisms.
These include microorganisms that ferment complex sub-
strates to simpler molecules; respiratory microorganisms
Published: 11 March 2009
BMC Genomics 2009, 10:103 doi:10.1186/1471-2164-10-103
Received: 28 October 2008
Accepted: 11 March 2009
This article is available from: http://www.biomedcentral.com/1471-2164/10/103
© 2009 Butler et al; licensee BioMed Central Ltd.
This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0),
which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Page 2
BMC Genomics 2009, 10:103 http://www.biomedcentral.com/1471-2164/10/103
Page 2 of 10
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that convert fermentation products to carbon dioxide
and/or methane; and syntrophic organisms that anaerobi-
cally oxidize some fermentation products and other sub-
strates in reactions that are only thermodynamically
feasible when respiratory organisms consume the syn-
trophs' products. The family Geobacteraceae has represent-
atives of all three metabolic groups, providing an
opportunity to evaluate how microorganisms might
evolve to fill these various niches in anaerobic ecosystems.
Within the Geobacteraceae, Geobacter and Desulfuromonas
are specialists in the complete oxidation of organic com-
pounds to carbon dioxide coupled to the reduction of
insoluble, extracellular electron acceptors [1]. In aquatic
sediments and submerged soils they influence the cycling
of carbon and metals by oxidizing acetate, the central fer-
mentation intermediate in anaerobic environments, with
the reduction of iron and manganese oxides [1,2]. In
Geobacter species can play an important role in the biore-
mediation of aromatic hydrocarbons by oxidizing the
contaminants with the reduction of Fe(III) oxides natu-
rally present in the subsurface [3,4]. This is a process
which can be artificially stimulated [5,6]. Another biore-
mediation application involving Geobacter species is to
add acetate to uranium-contaminated subsurface environ-
ments. This stimulates the growth of Geobacter species
which reduce soluble, mobile U(VI) to insoluble U(IV)
[7] and thus immobilize the uranium in situ [4,8]. The
ability of Geobacter and Desulfuromonas species to oxidize
organic compounds with electron transfer to graphite
electrodes provides a convenient method for harvesting
electricity from aquatic sediments and organic wastes to
power electronic devices [9-11].
subsurface environments
In contrast, the primary niche of Pelobacter species is
methanogenic environments, functioning either as fer-
mentative microorganisms or living in syntrophic associ-
ations with methanogens by partially oxidizing organic
compounds to hydrogen and acetate which the methano-
gens consume [12,13]. Pelobacter species cannot oxidize
acetate or other organic compounds completely to carbon
dioxide and are ineffective in electron transfer to metals
[14] or electrodes [15]. Therefore, not only the natural
environments, but also the technological applications of
Geobacter/Desulfuromonas versus Pelobacter species are
quite different.
Here we report on the sequenced genomes of six members
of the Geobacteraceae family: Geobacter sulfurreducens [16],
Geobacter metallireducens, Geobacter uraniireducens, Pelo-
bacter propionicus, Pelobacter carbinolicus, and Desulfurom-
onas acetoxidans. We use comparative genomics in an
effort to better understand the enzymes involved in these
unusual metabolisms, and to provide insight in to the
selective pressures that may have contributed to their evo-
Results and discussion
Identification of protein families in the six genomes
The general features of each of the six genomes are pre-
sented in Table 1. Orthologous proteins, those predicted
to have similar functions in the different organisms, were
identified by Markov clustering of sets of reciprocal best
BLAST matches [17]. Using all 21,716 protein coding
genes in the six genomes (see Additional file 1), 3,696
clusters with members from at least two genomes were
defined (see Additional file 2). 15,207 proteins (70.0%)
were classified into clusters. A functional role was pre-
dicted for each cluster using the G. sulfurreducens in silico
model annotation [18] and COG categorization [19].
The pattern of conservation of the proteins families across
all species (the phyletic pattern) was determined (see
Additional files 2 and 3). By far the most common pattern
was conservation across all species, 5,345 proteins were
members of clusters that included at least one protein
from each genome (see Additional file 3). The second
most common pattern was conservation in the Geobacter
species and P. propionicus only (1,158 proteins). Proteins
unique to the respiratory or fermentative species were rel-
atively rare. Only 370 proteins were found in the respira-
Table 1: General features of the Geobacteraceae genomes
Pelobacter propionicusPelobacter carbinolicus Desulfuromonas
Length (nt)
GC Content (%)
Protein coding
rRNA operons
13.8 kb
30.7 kb and 202.4 kb
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tory species but not the fermentative species (see
Additional file 4), and only 260 proteins were found in
the fermentative species but not the respiratory species
(see Additional file 5).
Whole-genome phylogeny
A phylogeny of the family was constructed using the 481
protein families that had a single protein from each of the
six genomes and the outgroup species Anaeromyxobacter
dehalogenans (see Additional file 6). These proteins had
diverse functions, including information storage, metabo-
lism, cell signaling, and unknown. The proteins from each
genome were concatenated then aligned, and this align-
ment was used to create a Bayseian model of the phylog-
eny (Figure 1). This analysis confirmed that, as
housekeeping-gene phylogeny suggests [20], the Geo-
bacteraceae can be divided into two clades, and that the
two fermentative Pelobacter species are not most closely
related to each other, instead there is one Pelobacter spe-
cies in each clade of the respiratory species (Figure 1).
Thus, based on phylogeny, there are at least three possibil-
ities for how modern Geobacteraceae evolved to fill multi-
ple metabolic niches. The ancestor may have been
adapted to a fermentative/syntrophic lifestyle with no reli-
ance on external electron acceptors. In this scenario, the
Geobacter and Desulfuromonas species would have inde-
pendently evolved strategies for the complete oxidation of
organic compounds coupled to Fe(III) reduction. Alterna-
tively, the ancestor may have been a respiratory microor-
ganism, and the Pelobacter species independently evolved
strategies for fermentation and syntrophy and lost the
ability to transfer electrons out of the cell. Another option
was that the ancestor may have had both types of metab-
olism, and the various branches of the family lost certain
abilities. We investigated these possibilities by analyzing
the conservation and evolutionary history of genes for
energy metabolism.
Conservation of pathways for acetate oxidation
In the respiratory species G. sulfurreducens, G. metalliredu-
cens, G. uraniireducens, and D. acetoxidans, acetate is the
primary electron donor and it is oxidized via the TCA
cycle, generating NADH, NADPH, and reduced ferredoxin
(Figure 2) [21-23]. In contrast, Pelobacter species are inca-
pable of acetate oxidation [12]. One protein family pre-
dicted to be acetate transporters (GSU0518) [24] was
conserved in all of the acetate-oxidizing species (see Addi-
tional file 7). However, neither this protein nor any of the
other acetate transporters found in G. sulfurreducens
(GSU1068, GSU1070, and GSU2352) were conserved in
either of the Pelobacter species (see Additional file 7).
Twenty one genes encode the enzymes of the TCA cycle
used by G. sulfurreducens [18] (Figure 2, see Additional file
7). There was full conservation in all of the respiratory
species of at least one copy of each of these enzymes (see
Genome-based Geobacteraceae phylogeny
Figure 1
Genome-based Geobacteraceae phylogeny. Bayesian
inference of the phylogenetic tree of the six Geobacteraceae
species discussed in the text, using another Deltaproteobacte-
rial species, Anaeromyxobacter dehalogenans, as the outgroup.
The tree was based on a concatenation of the proteins in the
481 families that had exactly one ortholog conserved in each
of the seven genomes (see Additional file 6). Values at branch
points are posterior probabilities.
The pathways of energy metabolism conserved in the respi- ratory Geobacteraceae species
Figure 2
The pathways of energy metabolism conserved in the
respiratory Geobacteraceae species. Shown are the
pathways, based those characterized in G. sulfurreducens, for
acetate activation and oxidation via the TCA cycle in the
cytoplasm, for inner membrane oxidation of TCA cycle
products coupled with electron and proton transport, and
for ATP generation. The genes encoding the enzymes of
these pathways and their conservation pattern in all of the
Geobacteraceae genomes are given in see Additional file 7.
The enzymes are colored black if there were orthologs for
every subunit in all of the respiratory species. The asterisk
indicates that malate dehydrogenase activity has been shown
in D. acetoxidans, though genes for the enzyme were not
found in the draft sequence of the genome. The pathway for
electron transfer through the periplasm and out to the
external electron acceptor is not well characterized in these
species, and is represented here by the three cytochromes
known to be required in vivo in G. sulfurreducens that are also
conserved in all of the respiratory species.
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Additional file 7). The one exception was the malate dehy-
drogenase in D. acetoxidans. There was no gene predicted
to encode a malate dehydrogenase in the incomplete ver-
sion of the genome, but this enzyme activity is found in
D. acetoxidans [23]. As with the acetate transporters, not all
of the genetic redundancy seen in G. sulfurreducens in the
enzymes of the TCA cycle was conserved across the family.
Only one copy of the aconitase (GSU1660) and the keto/
oxoacid ferredoxin oxidoreductase
GSU1862) were conserved in all the respiratory species
(see Additional file 7).
The Pelobacter species contained orthologs to many of the
TCA cycle enzymes (see Additional file 7), but there were
two notable exceptions. NADPH metabolism appears to
catalyzed by different enzymes in the Pelobacter species. A
monomeric-type isocitrate dehydrogenase (GSU1465)
was found in all of the respiratory species (see Additional
file 8), but was not conserved in either Pelobacter species
(see Additional file 7). In acetate oxidizers, this reaction is
the primary source of NADPH in the cell [25]. Instead, the
Pelobacter species contained non-orthologous isocitrate
dehydrogenase genes (Ppro_0452 and Pcar_1038 in clus-
ter 3107) of the more common, homodimeric type [25].
In addition, both Pelobacter species lacked the dehydroge-
nase (GSU0509–GSU0510) believed to transfer the elec-
trons from NADPH into the electron transport chain [26].
This enzyme was conserved in all four of the respiratory
species (see Additional file 7). These changes suggest that
the NADPH produced by the Pelobacter species may not be
used primarily as a source of electrons for energy metabo-
lism, as it is for the respiratory species. Furthermore, P.
carbinolicus contained a non-orthologous fumarase
enzyme (Pcar_0324) predicted to be of the class II, Fe(III)-
free type [27], rather than the class I, Fe(III) type found in
the other Geobacteraceae (GSU0994).
Conservation of pathways for extracellular electron
In the respiratory Geobacteraceae species, the reducing
equivalents from the TCA cycle are passed to inner mem-
brane quinones via NADH dehydrogenase (Figure 2) [21-
23]. This is predicted to be the only step in the electron
transport chain where protons are pumped across the
inner membrane for ATP generation [18]. G. sulfurreducens
encodes two NADH dehydrogenase operons, one with 12
subunits and one with 14 (see Additional file 7). The 14-
subunit enzyme is conserved in all of the respiratory spe-
cies and P. propionicus (see Additional file 7). In addition,
P. propionicus appears to have recently duplicated this
enzyme, there are three virtually identical copies in the
genome (Ppro_0628–Ppro_0641,
Ppro_1636, Ppro_3180–Ppro_3193). In contrast, P. car-
binolicus lacks the 14-subunit enzyme, but encodes an
ortholog to the 12-subunit enzyme (see Additional file 7).
This conservation pattern indicates that the 14-subunit
enzyme may be the more important for inner membrane
proton and electron transport; it is conserved in the four
respiratory species, and in the only fermentative species
predicted to use an NADH dehydrogenase (as described
below and in Figure 3).
The final part of the electron transport chain in the respi-
ratory species is transfer of electrons from the inner mem-
brane to cytochromes for transport to the cell surface. The
differences between the respiratory and fermentative spe-
cies are substantial in this part of the pathway. The
genomes of all four of the respiratory species contained at
least one copy of a putative cytochrome bc complex
(GSU2932–GSU2934), which is predicted to transfer elec-
trons from membrane-bound quinones to periplasmic
cytochromes [28] (Figure 2, see Additional file 7). Neither
of the Pelobacter species had any orthologs to this com-
plex. C-type cytochromes span the periplasm and outer
membrane in the respiratory species [1]. All of the Geo-
bacter and Desulfuromonas genomes contained more than
The pathways of energy metabolism in Pelobacter propionicus
and the differences from respiratory Geobacteraceae species
Figure 3
The pathways of energy metabolism in Pelobacter
propionicus and the differences from respiratory Geo-
bacteraceae species. Shown are the pathways of butane-
diol and acetoin fermentation used by P. propionicus.
Vertically-inherited enzymes with orthologs in the other Geo-
bacteraceae are shown in black. Both the vertically-inherited
NADH dehydrogenase and ATP synthase have been dupli-
cated in P. propionicus and these are shown in dark grey.
Enzymes acquired by lateral gene transfer are shown in red:
1) butanediol dehydrogenase, 2) acetoin dehydrogenase, 3)
pyruvate:ferredoxin oxidoreductase, 4) transcarboxylase,
and 5) methylmalonyl-CoA mutase, and an ATP synthase.
Enzymes conserved in the respiratory Geobacteraceae but
lost in P. propionicus are shown in white. Reactions with mul-
tiple enzymes encoded in the genome for which there are
diverse conservation patterns are shown as dashed arrows.
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100 ORFs that have the heme-binding motif [29] charac-
teristic of c-type cytochromes (see Additional file 1). Both
Pelobacter genomes had far fewer cytochrome genes, ca. 40
per genome (see Additional file 1). Many of the proteins
found only in the respiratory species were multi-heme, c-
type cytochromes (see Additional file 4), whereas none of
the proteins specific to the fermentative species were
multi-heme (see Additional file 5). In addition, both Pelo-
bacter species lacked most of the specific cytochromes
required for electron transfer in G. sulfurreducens in vivo.
These include those conserved in all of the respiratory spe-
cies: MacA, a c-type cytochrome associated with the inner
membrane [30] and OmcB, an outer-membrane cyto-
chrome [31].
Lateral transfer of fermentation genes
Thus, while the Pelobacter species contained many verti-
cally-inherited genes for respiratory metabolism, several
key enzymes are different or missing in both species. To
investigate evolution of the fermentative and syntrophic
metabolism, Pelobacter-specific genes were analyzed, and
genes originating from lateral gene transfer were identi-
fied using a combination of phylogenetic and BLAST-
based analysis (see Additional file 9). Both Pelobacter spe-
cies catabolize butanediol and acetoin [12]. The butane-
diol dehydrogenase (Bdh, Pcar_0330) and acetoin
dehydrogenase (AcoABCL, Pcar_0343–Pcar0346), which
catalyze the initial steps in the metabolism of these com-
pounds, have been characterized in P. carbinolicus [32]. P.
propionicus has genes with high sequence similarity to
these, but the operon structure of the putative acetoin
dehydrogenase included a duplication of the A and B sub-
units (Bdh, Ppro_1043 and AcoABCABL, Ppro_1024–
Ppro1029, see Additional file 1). Phylogenetic analysis
showed that the most closely related enzymes are not
from Geobacter or Desulfuromonas, nor any other delta-Pro-
teobacteria species (see Additional file 10). Instead the
Pelobacter genes were most closely related to the butane-
diol catabolic genes from Pseudomonas [33] and Gram-
positive species, indicating that these genes originated
from lateral gene transfer (see Additional file 10).
The subsequent steps in the catabolism of the acetyl-CoA
and acetaldehyde from acetoin are markedly different in
the two Pelobacter species. The pathway in P. propionicus is
cyclic and requires membrane-bound electron transport
enzymes (Figure 3) [34]. Several of the key enzymes were
predicted to have been acquired by lateral gene transfer.
Pyruvate:ferredoxin oxidoreductase is required to convert
acetyl-CoA to pyruvate (Figure 3), and there were two het-
erotetrameric pyruvate:ferredoxin oxidoreductases from
lateral gene transfer. One (Ppro_0322–Ppro_0325, see
Additional file 1) is most closely related to the enzymes
from Clostridia tetani and Thermotoga species, and the
other (Ppro_0469–Ppro_0472, see Additional file 1) is
most similar to the enzyme in Syntrophobacter and several
archaeal species.
Pyruvate is then converted to succinyl-CoA to regenerate
NAD+ without the need for a cooperating hydrogen-oxi-
dizing species (Figure 3). P. propionicus has orthologs of
four TCA cycle enzymes and the NADH dehydrogenase
from the respiratory Geobacteraceae that could carry out
these reactions (Figure 3, see Additional file 7). Then, pro-
pionate is generated via a methylmalonyl-CoA mutase
and transcarboxylase (Figure 3). Both of these enzyme
were predicted to have been acquired from lateral gene
transfer. The mutase (Ppro_1284–Ppro_1285, see Addi-
tional file 1) is related to enzymes from Chlorflexus and
Geobacillus species, and the transcarboxylase (Ppro_0033–
Ppro_0034, see Additional file 1) is related to that crystal-
lized from Propionibacterium freudenreichii [35].
Thus, it appears that P. propionicus uses a mosaic of verti-
cally inherited and laterally acquired genes for fermenta-
tion. Interestingly, the pathway uses a complete, vertically
inherited, respiratory electron transport chain – the succi-
nate dehydrogenase operates in reverse as a fumarate
reductase, accepting reducing equivalents from the NADH
dehydrogenase [34]. This is equivalent to that used by
Geobacter species growing by fumarate respiration [18,36].
Differences between Pelobacter species associated with
P. carbinolicus ferments via much simpler pathway of cyto-
plasmic enzymes (Figure 4). As described above, the
butanediol dehydrogenase and acetoin dehydrogenase
appear to have been acquired by lateral gene transfer.
NAD+ is regenerated either by ethanol production or by
proton reduction to hydrogen, which requires a syn-
trophic partner and ATP is made by substrate level phos-
phorylation by an acetate kinase [12].
Some Pelobacter species live in syntrophic associations
with methanogens by partially oxidizing organic com-
pounds to hydrogen and acetate which the methanogens
consume [12,13]. Both Pelobacter species lacked orthologs
to any of the Geobacter-type [37] hydrogenases
GSU2420 or GSU2718–GSU2722, see Additional file 1).
Furthermore, the hydrogenases in the two Pelobacter spe-
cies are dissimilar. This may reflect the fact that P. carbino-
licus is capable of growing syntrophically with a hydrogen-
consuming partner, most typically a methanogen [12].
Reducing equivalents can be disposed with the produc-
tion of hydrogen, as long as the methanogen maintains
hydrogen concentrations low enough for hydrogen pro-
duction to be thermodynamically favorable. P. propionicus
does not grow in this manner [12]. P. carbinolicus has two
highly-similar, four-subunit hydrogenases (Pcar_1602–
Pcar_1605 and Pcar_1633–Pcar_1636) related to the

subset: commoncrawl


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NHL amends unsportsmanlike conduct rule in response to Avery's antics
Updated: April 14, 2008, 6:38 PM ETAssociated Press
NEW YORK -- Sean Avery found yet another way to annoy Martin Brodeur -- and forced the NHL to change a rule in his honor.
The Hall of Fame resume of the New Jersey Devils goalie doesn't resonate with Avery, the New York Rangers forward who has turned agitation into an art form. During a 5-on-3 power play in New Jersey's 4-3 overtime playoff victory Sunday night, Avery planted himself in the crease and faceguarded Brodeur.
Holding his stick upward, Avery waved it side to side ...
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Pace Analytical Lab Technician Interview Questions
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I applied through a recruiter. The process took 1+ week. I interviewed at Pace Analytical.
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Interview Questions
- Asked if I could handle working in an incredibly fast-paced, high turn-around environment. Should have given example of ability to do so Answer Question
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Lab Technician InterviewAccepted OfferNegative ExperienceEasy Interview
I applied online. I interviewed at Pace Analytical (Minneapolis, MN) in July 2012.
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Interview Questions
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Reviews - Hilton Warwick / Stratford-upon-Avon4
Junction 15, M40 A429 Stratford Road, Warwick, CV34 6RE
Price From £120View Rooms
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Very Good
72% would recommend it to a friend
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Very good stay, fair value for money.
Absolutely no complaints with regards to the staff, quality of service or the food.
The rooms are fairly expensive so do not give good value for money though. But your money does get you a quality room and excellent service!
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Expensive and in dire need of renovation
They had had "system problems" meaning that our confirmed booking hadn't been received by them meaning they had no rooms for us.
They offered us Coventry Hilton instead, we refused this and eventually they found us two rooms. We were offered a free drink as compensation. This hotel is tired and in desperate need of renovation. One of our rooms was affected by a noisy wedding. A poor experience.
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Booked on late rooms and specified a non-smoking room.
They had given all of their non-smoking rooms away. I was travelling late at night (arriving at 1.00am) and as a smoking room was not acceptable to me, I had to travel for a further 30 minutes to another hotel that had availability in Bromsgrove. Exhausting and disappointing experience!
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Hilton Warwick / Stratford-upon-Avon
Just perfect for our needs.
Great value would definitely use again and recommend.
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Mind Blowing !!
You are excellent and i hope you continue to stay this way....100%
Superb Visit
Cant fault anything about my visit/stay at the end of last year.
Everything about it was spot on and I would absolutely return in the future. 100% recommend
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All a bit tired.
Room was very dated and tired.
You should not have to pay for extras such as parking and WiFi and £4.80 for a medium cappuccino is a rip off.
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Nice enough, but expensive for what it is
The rooms are a little dated, but they're clean and nice enough.
Staff are pleasant and very helpful. I just think their prices are too high for what you get and there are better value, nicer hotels in the area. The thing that really grates is their inexcusable, ridiculous charges for sundries during your stay. Everything you touch seems to have a hefty price tag attached, including the wifi and water in your room and it just leaves you with a bit of a sour taste in your mouth when you pay the bill at the end. It's a reasonable option when other hotels in the area are full, but it would be far from my first choice.
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Good place to stay
Hotel gave a good first impression, relaxing atmosphere and smart decor.
Everything you would want in your room and some good complimentary touches. Breakfast excellent super choice and good quality. Only complaint would be not quite sure why you have to pay for parking when it is not walking distance from a town!
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Good quality chain hotel shame pool closed
The hotel was very clean.
Had everything you need except a plug near a mirror to dry your hair.
Staff polite and functional rather than friendly and welcoming. The pool is closed and not being replaced this would make me think twice about staying here again
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Jimmy Wales and Palestine
January 12, 2012
ByJoey Ayoub I've had a discussion with Jimmy "Jimbo" Wales, the co-founder of Wikipedia, concerning the fact that he was participating in the Israeli Presidential Conference despite the international call of the BDS (Boycott, Divestment and Sanctions) Movement. Thought I'd share it with you. I'll talk more about the Palestinian


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1929 rolls-royce phantom ii boat-tail ex Read more
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Days Inn & Suites Groton Near the Casinos hotel raises the stakes on value in a great coastal setting. Centrally located between New York City and Boston, our Groton, CT, hotel near Foxwoods Resort Casino is right off Interstate 95, three miles from the US Naval Submarine Base, and close to exciting hotspots like the MGM Casino and Mohegan Sun Casino, as well as beaches and shopping. Count on comfortable accommodations and modern amenities like a microwave and refrigerator to make your stay exceptional. Fuel up with free Daybreak continental breakfast each morning and surf the Web with free Wi-Fi Internet access. Our Groton, CT, hotel offers guest laundry facilities and a business center and our refreshing outdoor pool is a great place to revitalize your energy after a long day. Non-smoking and handicapped-accessible rooms are available and kids 17 and under stay free with an adult. Book a Jacuzzi suite for extra comfort. LOCAL ATTRACTIONS With six casinos jam-packed with slots and table games, you can spend hours on end at Foxwoods Resort Casino, just minutes from our Groton, CT, hotel. While you are there, head next door to get a taste of Native American culture and natural history at Pequot Museum. Surround yourself with gourmet dining, upscale shops and live entertainment at Mohegan Sun Casino, just 12 miles away. Climb aboard historic tall ships and stroll through a re-created 19th-century coastal village at Mystic Seaport. Take a 25-mile drive to Clinton Crossing Premium Outlet and fuel your shopping spirit with big savings on brand names. Soak up the sun at Ocean Park Beach or cruise on an Essex Steam Train and Riverboat. DINING OPTIONS Enjoy fresh, innovative dishes at Olio Restaurant, or dig into home-style cooking at The Spot. Savor tasty burgers at Five Guys or head to familiar favorite Applebee's where our guests receive a 10% discount, all near our hotel in Groton, CT. BUSINESS AND EVENT FACILITIES Fax and copy service is available.Wyndham Hotel Group
24 hour front desk
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Showtec Expression 16000 Spot
CMY color mixing Frost / Iris / Focus / Zoom / Prism Two Rotating Gobo Wheels + Effect wheel 12000 LumenThe Expression 16000 Spot is an extremely powerful LED movinghead with a 360W LED source. It offers a professional alternative to a 1200W HID spot with an output over 12000 lumen and an incredible peak intensity of 256000cd. The Expression 16000 spot is equipped with 2 rotating Gobo wheels, one static Gobo wheel, 7 dichroic filter + white Color wheel, Frost, Iris, Focus, Zoom and Prism, so it has a lot of functionality to make a creative lightshow. Especially the Zoom combining with the Prism wheel and the impressive LED output produces a powerful and very large effect output. The Expression 16000 Spot combining with the unique single module of 360W light source is determined to set the new lighting standard for LED lighting technology.
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Showtec Phantom 140 LED Spot
110W LED source 7 Rotating Gobos & 8 Colors 16 Built-in programs selectable by DMX Menu on Full color display Motorized focusThe Phantom 140 Spot is the ´middleman´ in our successful Phantom series. It has more output power compared to the Phantom 75, and is lighter and more compact compared to the Phantom 225. Equipped with beautiful full color display and professional finish. It houses a high efficient 110W LED source, high efficient optics for maximizing the output, 8 colors, 7 gobo´s, motorized focus, 3-facet prism, electronic dimmer and fast strobe.
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Motorized Zoom Motorized Focus 8 Replaceable gobo's & 8 colors Gobo shake, gobo rotate and 3-fact prism 16 Built-in programs selectable by DMXThe Phantom 95 Spot is a mid-sized moving head equipped with a 95W LED Light source. It offer numerous functions at an affordable price level. It offers motorized focus and zoom ensuring razor sharp gobo and beam effects in any circumstance.It contains a gobo wheel with 7 gobo's and a colour wheel with 8 vivid colours.With the electronic zoom function the zoom can be controlled within a range of 9° to 16,5°The Phantom 95 Spot is without doubt the right solution for mobile DJ, clubs and rental companies.
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24.500 Lux @ 1 M 7 Rotating Gobos & 8 Colors 16 Built-in programs selectable by DMX Gobo shake, gobo rotate and 3-facet prism Motorized focusThe Phantom 75 LED spot is a medium size powerful moving head with a 75W white LED light-source. It is very complete with 7 Gobo's, 8 dichroic filters and lots of extra functionalities like gobo-shake, gobo-rotate, prism, split & rainbow colors. Because of the LED source the shutter is electronic not mechanical. Focus is motorized and it has a mechanical zoom. You can choose between a 8 or a 14 DMX channel personality. If you like to operate without controller you can use the 16 built-in programs which can run automatically, sound-active or in master/slave mode. The stylish design and lightweight housing make this moving head very attractive and ergonomic. The gobos can be changed very easily by a handy lid. Check the online product video for more details.
Showtec Phantom 75 LED Spot
GE CP81 240V 300W GY9.5 FSK Fits Arri Junior 300Wattage: 300WVoltage: 240VBase: GY9.5Average life: 50hrColour temperature: 3200kLuminous flux: 6900lm
Showtec Helicopter 4 LED
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Allen Key Toplok
A genuine Litestructures allen key for use with Taperlok equipped LiteDeck.
Backstage Warehouse Metallic Confetti Rectangles - Gold
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Lamp Holder HPL575 ( Source 4)
Lamp holder for HPL lampsRated voltage: 250VRated current: 16AOperating temperature: 350CHolder: ceramic unenclosedConnection lead: H05SJ-K 1.5mmLength: 137mmFixing: push on connectorThe unique design and material combination of the contacts reduces the generation of thermal energy and is designed to withstand high temperatures.
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Online Catalogue | Lighting | Controllers and Desk | Software Control Systems | Showtec Sweetlight
The interface "Cable" allows to discover an "entry level" version of our software,for a very low price. USB - DMX cable led for dmx output max 100 dmx channels max 10 fixtures 3D rendering only while interface is not connected max 20 scenes running together software downloadable from internetBe aware that the Sweetlight USB cable has no groundloop protection. To be sure that you don't damage the cable if a groundloop occurs use a showtec DMX booster, ordercode: 50346, 50347 or 50780. Sweetlight D512 and Remote have built-in groundloop protection.
The interface "D512" allows to use our software without any restriction,with 512 DMS channels. Metal casing 2 LED's in front panel (power and USB link) USB link with computer DMX output for lighting equipment Thermal protection on DMX groundThis interface can play a "dynamic" scene for 512 DMX channels, without computer.
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STAY Taipei (Simple Table Allléno Yannick)January 27, 2012French • Taipei, Taiwan
Unlimited supply of Lalos bread!
Unlimited supply of Lalos bread!
Try to rent a bike to ride around the lake. Enjoy the view, the breeze, and the exercise!
Really nice buffet and great selection of pastry!
the le sportsac at terminal 2 duty free is at least 20% off versus the prices in the city.


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This project will provide the capital to expand the only grocery store serving eight villages in Guatemala, selling basic staples to over 850 families. Profits go to scholarships for local youth.
What is the issue, problem, or challenge?
The 850 indigenous families that live in the eight villages surrounding Los Jometes, Guatemala, must travel far to get basic goods such as laundry soap, medicines and crop fertilizers. Local children do not have access to school supplies and often cannot pay school fees. This project will expand a grocery store so that it can provide these goods to the families. Profits will provide scholarships to at least 20 children from poor families.
How will this project solve this problem?
Expand the types of medicines, food and housewares at store. Make school supplies available at an affordable cost. Identify children with the greatest need and motivation; use store profits to pay for their school fees, uniforms and books.
Potential Long Term Impact
The store will provide essential goods to eight villages. The school-supply section will make education more accessible to children who otherwise cannot go to school for lack of pencils and notepads. The scholarships will benefit needy children.
Funding Information
Total Funding Received to Date: $0
Funding Information
This project is now in implementation and no longer available for funding. Received funds will be used to accomplish concrete objectives as indicated in the project's "Activities" section. Updates will be posted under the "Project Report" tab as they become available.
Donors' contributions and pledges to this project totaled $0 . The original project funding goal was $14,300.
Additional Documentation
This project has provided additional documentation in a Microsoft Word file (projdoc.doc).


text:
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Page 1
Three-dimensional structure of basal body triplet
revealed by electron cryo-tomography
Sam Li1,3, Jose-Jesus Fernandez2,
Wallace F Marshall3and David A Agard1,3,*
1The Howard Hughes Medical Institute, University of California,
San Francisco, CA, USA,2Centro Nacional de Biotecnologia—CSIC,
Campus Universidad Autonoma, Madrid, Spain and3Department of
Biochemistry and Biophysics, University of California, San Francisco,
Basal bodies and centrioles play central roles in micro-
tubule (MT)-organizing centres within many eukaryotes.
They share a barrel-shaped cylindrical structure composed
of nine MT triplet blades. Here, we report the structure of
the basal body triplet at 33A˚ resolution obtained by
electron cryo-tomography and 3D subtomogram aver-
aging. By fitting the atomic structure of tubulin into the
EM density, we built a pseudo-atomic model of the tubulin
protofilaments at the core of the triplet. The 3D density
map reveals additional densities that represent non-tubu-
lin proteins attached to the triplet, including a large inner
circular structure in the basal body lumen, which func-
tions as a scaffold to stabilize the entire basal body barrel.
We found clear longitudinal structural variations along
the basal body, suggesting a sequential and coordinated
assembly mechanism. We propose a model in which
d-tubulin and other components participate in the assem-
bly of the basal body.
The EMBO Journal (2012) 31, 552–562. doi:10.1038/
emboj.2011.460; Published online 13 December 2011
Subject Categories: cell & tissue architecture; structural biology
Keywords: basal body; centriole; Chlamydomonas reinhardtii;
electron cryo-tomography; three-dimensional reconstruction
The basal body, as a cellular organelle for organizing micro-
tubules (MTs), is composed of nine MT triplet blades.
It carries out multiple essential functions in cellular pro-
cesses. During cell division, it functions as a centriole to
recruit pericentriolar material to form the centrosome, which
in turn is responsible for establishing the bipolar spindle
during mitosis. Although centrioles are dispensable for mi-
tosis in certain organisms and cell lines (Debec et al, 2010),
ample evidence shows that in many other cases, over-ampli-
fication or depletion of centrioles leads to a delay in cell
division, aneuploidy and cell death, suggesting their impor-
tance for normal mitosis (Hinchcliffe et al, 2001; Piel et al,
2001; Mikule et al, 2007). More importantly, the centriole is
responsible for establishing cell polarity during cell division
(Yamashita et al, 2007; Wang et al, 2009). In many quiescent
cells, the centriole will migrate to the cell periphery, and
anchor beneath the cell membrane as a basal body that
templates cilium formation. The basal body also provides a
docking site for intraflagellar transport particles that move
bidirectionally along the cilium (Deane et al, 2001). Recent
studies show that, in addition to its role in motility, the cilium
also functions as an antenna for communicating between the
intracellular and external environment of the cell and plays
essential roles during cell regulation, tissue differentiation
and embryonicdevelopment
Mutations in cilium or basal body genes result in various
forms of human disease, collectively known as ciliopathies
(Gerdes et al, 2009).
Biogenesis of the centriole and basal body has been
studied in a variety of model organisms (Ringo, 1967;
Dippell, 1968; Allen, 1969; Anderson and Brenner, 1971;
Anderson, 1972; Cavalier-Smith, 1974; Gonza ´lez et al, 1998;
Pelletier et al, 2006; Giddings et al, 2010; Guichard et al,
2010). Genes involved in centriole biogenesis, either regula-
tory or structural, are generally well conserved, suggesting a
common assembly pathway across species (Carvalho-Santos
et al, 2010). The biogenesis of basal bodies or centrioles is
tightly coupled to the cell cycle, suggesting a highly regulated
assembly mechanism (Doxsey et al, 2005).
Proteomic studies of purified basal bodies or centrioles have
identified a list of bona fide centriole components and basal
body specific proteins many of whose function and structure
remain unknown (Andersen et al, 2003; Li et al, 2004; Keller
et al, 2005; Kilburn et al, 2007). Despite extensive descriptions
of the centriole and basal body ultrastructure, the lack of high-
resolution structural information significantly limits our under-
standing of the assembly process and the full repertoire of
cellular functions for this complex organelle.
Here,we used electron
to visualize basal bodies purified from Chlamydomonas
reinhardtii in a near-native state. In combination with a
subtomogram averaging strategy, it has been possible to
obtain a high-quality 3D reconstruction of the basal body
that offers insight on how tubulin protofilaments (PFs) and
accessory components assemble into the triplet. Based on our
structural findings and previous studies, we propose potential
locations for several basal body components. Our structure
provides a framework for understanding the molecular me-
chanism of basal body and centriole biogenesis, and for
integrating new information as the protein composition of
the non-MT components are elucidated.
(Nigg andRaff, 2009).
cryo-tomography (cryo-ET)
Overall structure of the basal body triplet
Purified basal bodies in near-native state were visualized by
cryo-ET. In most of the tomograms, two cylindrically shaped
Received: 14 August 2011; accepted: 15 November 2011; published
online: 13 December 2011
*Corresponding author. Department of Biochemistry and Biophysics,
Howard Hughes Medical Institute, University of California at San
Francisco, 600 16th Street, Room S412D, San Francisco, CA 94158-2517,
USA. Tel.: þ1 415 476 2521; Fax: þ1 415 476 1902;
E-mail: firstname.lastname@example.com
The EMBO Journal (2012) 31, 552–562|& 2012 European Molecular Biology Organization|Some Rights Reserved 0261-4189/12
The EMBO Journal VOL 31|NO 3|2012
&2012 European Molecular Biology Organization
Page 2
basal bodies were visible since they are tethered laterally
by the distal striated fibres (Hoops et al, 1984). The basal
bodies have a reproducible size, with an average diameter
of 260nm and an overall length of 600nm (Figure 1A). The
MT triplets start from the proximal end (the bottom in
Figure 1A) and span about 400nm longitudinally towards
the distal end where the C-tubules of the triplets terminate.
The A- and B-tubules continue as a doublet for about 150nm
before they reach the transitional plate, a hallmark of the
transition zone where the axoneme will assemble (Cavalier-
Smith, 1974; O'Toole et al, 2003; Geimer and Melkonian,
2004). We did not observe the cartwheel structures in our
tomograms, presumably because they were lost during pur-
ification. Electron dense structures, known as 'A-tubule feet',
are consistently visible in our tomograms along the wall of
the triplets projecting towards the lumen (Cavalier-Smith,
1974; Geimer and Melkonian, 2004), showing characteristic
8- and 16-nm periodicity (Figure 1A). The region decorated
with A-tubule feet starts at about 100nm from the triplet
minus (proximal) end, spans about 250nm longitudinally
and terminates at about 45nm before the triplets become
doublets. This section forms the central core of the basal
body and was used for tomogram subvolume averaging
in order to obtain a higher-resolution structure of the
basal body.
We obtained an averaged MT triplet at 33A˚ resolution
(Figure 1B; Supplementary Figure S1). The resolution of the
averaged structure is sufficiently high to allow us to discern
each PF in the longitudinal projection of the triplet (Figure 1B
and C). The A-tubule is a complete MT composed of 13 PFs,
numbering starts clockwise from the basal body luminal side
as A1 to A13 following the Tilney-Linck convention (Linck
and Stephens, 2007). PF A10 is the site where the B-tubule
joins with the A-tubule. PFs A10 to A13 are referred to as
partition PFs shared between A- and B-tubule. The B-tubule is
composed of 10 PFs that are numbered from the outside
surface of the triplet clockwise as B1 to B10. The C-tubule
also has 10 PFs. PF C1 starts as a branch from PF B4 and they
Figure 1 Cryo-ET reconstruction of the basal body triplet. (A) A cross-section of tomographic reconstructed volume containing a basal body.
The section is through the centre of the basal body barrel. The proximal end is at the bottom and the distal end is at the top. The 'A-tubule feet'
are marked with *. The terms of probasal body, A-tubule feet and transitional plate follow conventions of Geimer and Melkonian (2004).
(B) The averaged 3D structure of the basal body triplet viewed from the distal end. The MT triplet density map has been deposited in the
Electron Microscopy Data Bank with accession code EMD-5252. (C) A longitudinal projection of a 16-nm section of the averaged triplet. Every
other PFs in the triplet are labelled. (D) Docking of crystal structure of tubulin into the triplet density map. Selected PFs are labelled. The
locations of the highest curvature in the A-tubule are marked with *.
Electron cryo-tomography of basal body triplet
S Li et al
&2012 European Molecular Biology OrganizationThe EMBO JournalVOL 31|NO 3|2012 553
Page 3
are numbered clockwise as C1 to C10. PFs B5 to B8 form the
partition shared by the B- and C-tubules.
The A-tubule has an elliptical shape with a substantial
variation of curvature along the MT wall (Figure 1B and C).
The longest axis running across the internal diameter of the
A-tubule is between PFs A3 and A10 with a diameter of
B247A˚. The shortest axis is B201A˚between PFs A6 and
A13. This change of diameters is equivalent to a 10% distor-
tion of an intact 13-PF MTand is similar to the A-tubule in the
axoneme doublet where B8% distortion has been observed
(Sui and Downing, 2006). Interestingly, the variation of
curvature is non-isotropic along the wall of the A-tubule.
The highest curvature is at PFs A9 and A10, followed by the
next-highest curvature at PFs A2 and A3, where large lateral
gaps are observed between PFs. The smallest curvature is at
the partition site from A11 to A13. In contrast to the A-tubule,
the B- and C-tubules have a rather smooth and uniform
curvature with diameters about 260A˚. The diameter and
the curvature of the B- and C-tubules indicate that both
would form a circular MT with 15 PFs if they formed
complete rings, similar to the B-tubule in the axoneme
doublet (Sui and Downing, 2006).
Building a pseudo-atomic model of the triplet
In our structure, the 4-nm periodicity between individual
tubulin monomers can be easily resolved along most of the
PFs of the basal body (Supplementary Figure S2). The z-rise
(longitudinal rise) of tubulins between adjacent PFs, varies
from 10 to 12A˚, consistent with previous theoretical and
experimental data from MTs with different PF numbers
(Chre ´tien and Wade, 1991; Sui and Downing, 2010). This
allowed us to fit the atomic structure of a/b tubulin into the
EM density map and build a pseudo-atomic model of the
tubulin core of the triplet (Figure 1D). Previous studies have
shown that in a/b tubulin, the M-loop and H1-S2/H2-S3
loops provide the main lateral interactions between adjacent
PFs and we have kept these contacts in our model (Nogales
et al, 1999; Li et al, 2002; Sui and Downing, 2010). The overall
fit is excellent at the current resolution. In the A-tubule, due
to the variation in local curvature, the closest lateral interac-
tions are within partition PFs A11 to A13. Conversely, the
interfaces between PFs A2/A3 and PFs A9/A10 have less
contact due to large local curvature.
The fitting of tubulin PFs into the B- and C-tubule density
resulted in uniform tubulin lateral interactions. We have
modelled PF B1 as a tubulin PF that makes unusual lateral
contact with the outside surface of PF A10. Since the distal
half of PF C1 exhibits an 8-nm interval with a gap (Figure 4A
and B), it is most likely occupied by non-tubulin protein in
this region. Therefore, we did not fit tubulin monomers into
the PF C1 position anywhere along its length. This long-
itudinal change in PF C1 will be described in detail below.
Non-tubulin components associated with the triplet
Proteomic studies have shown that, besides tubulin, the basal
body contains nearly 50 non-tubulin components (Keller
et al, 2005). In order to find where they bind, how the tubules
are associated to form a triplet and how the triplets are
connected in the basal body, we used the pseudo-atomic
model of the tubulins within the triplet as a mask to subtract
its density from the 3D density map. The resulting difference
map shows novel density features that must correspond to
the locations of most of the non-tubulin accessory proteins
(Figure 2A).
Just as in the axoneme doublet structure (Nicastro et al,
2006; Sui and Downing, 2006), we also observed densities
decorating on the internal wall of A- and B-tubules in the
triplet, but in a more asymmetric manner. In the A- and B-
tubule, there are filamentous densities running across PFs A1
to A4 and B4 to B6, respectively, with an 8-nm periodicity
(Figure 2B and C). The densities follow the rise of the tubulin
helical repeat inside the lumen, forming lateral cross-links
between neighbouring tubulin monomers at the lumen side.
Likely, these are Tektin family proteins that stabilize adjacent
PFs and fine-tune local curvature of the tubule (Amos, 2008).
We also observed a cone-shaped density attached on the
luminal side of PF A5 with 8-nm periodicity (* in
Figure 2A), likely to stabilize the A-tubule or as the part of
structure connecting to the neighbouring triplet. Interestingly,
similar density has been consistently observed in the axo-
neme doublet (Nicastro et al, 2006; Sui and Downing, 2006;
Movassagh et al, 2010). Across from the cone-shaped density,
at PF A6 a stub-like density projects out every 8nm on the
outside wall of the A-tubule (Figure 2A). The stub connects to
the C-tubule from the neighbouring triplet and will be de-
scribed in detail in the next section. Meanwhile, density was
observed on the outside wall of the A-tubule running across
PFs A8 to A10 with an 8-nm longitudinal spacing (Figure 2D).
Since both PFs A10 and B1 are at the junction of A- and B-
tubules, this density presumably will stabilize the linkage
between the A- and B-tubules at the outside wall of triplet.
Remarkably, a large Y-shaped density was observed lying
horizontally as a ridge along the luminal side of the A- and B-
tubules (Figures 2A and 3A). It spans about 380A˚, nearly the
entire inner circumference of the A- and B-tubules. It projects
radially about 170A˚ towards the centre of the basal body
barrel. The estimated mass of this structure is 1.1MDa. We
have divided this structure into four parts and assigned them
as a central stem with three arms, termed armA, armB and
armC (Figure 3A and B). The central stem binds directly to
both A- and B-tubule. On the right side in Figure 3A, it fits into
the groove between PFs A1 and A2, which is likely the position
of the seam in the A-tubule (Song and Mandelkow, 1995).
After rising longitudinally B40A˚, the left side of the stem
binds to PF B10 in the B-tubule. Here, the stem extends
laterally, running across the entire outer surface of PF B10
and partial surface of PF B9. Together, this central stem fills in
the gap between the A- and B-tubule and cross-links the two
tubules at their closest distance (B82A˚). It makes substantial
interactions with both tubules at their luminal joint, with an
estimated total contact area between the stem and the A- and
B-tubule of B5200A˚2. Multiple copies of the stem stack long-
itudinally with an axial repeat of 8nm, forming a left-handed
spiral-shaped filament viewed from the outside of the basal
body (Figure 3A). This filament might account for the 11th PF
of the B-tubule as previously observed (Tilney et al, 1973).
ArmA rotates about 1081 counterclockwise relative to the
stem and extends 190A˚ towards the direction of A-tubule
(Figure 3A and B). At its end, armA connects longitudinally to
the neighbouring armAs, resulting in a filament along the
basal body barrel with an 8-nm periodicity. ArmB is 210A˚
long and it is about 1151 clockwise relative to the stem
(Figure 3A). At the end of armB, the neighbouring two
arms join, forming in a bifurcated structure with 16-nm
Electron cryo-tomography of basal body triplet
S Li et al
The EMBO JournalVOL 31|NO 3|2012
&2012 European Molecular Biology Organization
Page 4
periodicity (Figure 3B). This contributes to the 16-nm axial
repeat pattern projecting towards the lumen of the basal body
barrel as observed in the tomograms (Figure 1A). ArmC is
branched 901 from the armB, with a hook-shaped structure.
Like armA, a stack of armC also connects longitudinally to
form a filament with 8-nm periodicity (Figure 3A). In con-
clusion, this large Y-shaped structure forms a scaffold on the
luminal side of the basal body cross-linking and probably
stabilizing both A- and B-tubule.
In addition to the large density that connects the A- and B-
tubules as described above, we also observed relative weak
filamentous densities that connect PFs B10 and A13 on the
inside of the tubule structure (Figures 2A and 3C). The
connection, which spans about 90A˚, forms a ladder with 4-
nm periodicity. Each rung of the ladder is tilted, with a rise
about 4nm from one end at PF B10 to the other end at PFA13,
further stabilizing the linkage between A- and B-tubule.
Longitudinal structural variations along the basal body
To reveal the structural variations of the basal body, we have
divided the triplet subvolumes into eight groups according to
their longitudinal positions. Only subvolumes within each
group were averaged (Figure 4A). To our surprise, groups
from the proximal half of basal body (groups 1–4) have
distinct structural variations compared with the groups
from the distal half (groups 5–8). The variations mainly
reside on the C-tubule. From group 4 to group 5, there is an
emergence of density in the lumen of the C-tubule. In addi-
tion, the periodicity at PF C1 changes from 4 to 8nm.
To analyse these changes in greater detail, we re-divided
the subvolumes into two groups, the proximal half (sum of
972 subvolumes from groups 1–4) and the distal half (sum of
972 subvolumes from groups 5–8) and recalculated their
averaged structure, respectively. The resulting two EM den-
sity maps, as shown in Figure 4B, show significant differ-
ences. In the proximal half, the C1 PF, like any other MT PFs
in the C-tubule, exhibits a 4-nm axial repeat. In contrast, the
distal half has longitudinally disconnected density with 8-nm
periodicity. In addition, the density with 8-nm spacing at C1
extends further laterally across the outside surface of PF C2,
C3 and C4, forming a continuous hook-shaped arm with an
estimated mass of 270kDa. This arm forms a stable linker
between the B- and C-tubules at the outside surface of the
basal body.
The distal half of the basal body additionally contains a
stack of crescent-shaped filamentous structures (Figure 4C).
These filaments span B136A˚in the lumen of the C-tubule.
One end of the filament anchors to PF C3, while the other end
Figure 2 Non-tubulin densities associated with the basal body triplet. (A) A calculated difference map based on the pseudo-atomic model of the
triplet. The density contributed by tubulin is coloured in blue and the non-tubulin proteins associated with the triplet are coloured in yellow.
Selected PFs are labelled. The arrow points to the second A- and B-tubule linker connecting PFs A13 and B10. A cone-like structure in the lumen of
the A-tubule is marked with *. (B) Filamentous structure associated in the luminal wall of the A-tubule. The filaments attached to the luminal side
of A-tubule are highlighted in yellow. They are running across PFs A1 to A4, with 8-nm periodicity. The tubulin helices in the A-tubule are
indicated with red arrows. (C) Filamentous structure associated on the luminal wall of the B-tubule. The densities are running across PFs B4 to B6,
with 8-nm periodicity. The tubulin helices in the B-tubule are indicated with red arrows. (D) Densities are observed on the outside wall of the
A-tubule, running across PFs A8 to A10 with a longitudinal spacing of every 8nm. The red arrows indicate tubulin helices in the A-tubule.
Electron cryo-tomography of basal body triplet
S Li et al
&2012 European Molecular Biology OrganizationThe EMBO JournalVOL 31|NO 3|2012 555
Page 5
attaches to the junction between PFs C6 and C7. The esti-
mated mass of this elongated filament is about 46kDa.
Interestingly, the filament is tilted and descends about 20A˚
running from PF C3 to PFs C6/C7. Assuming the triplet C-
tubule has the MT B-surface lattice and can be seen as a
bundle of tubulin helices (red arrows in Figure 4C) (Chre ´tien
and Wade, 1991; Song and Mandelkow, 1995), the tilting of
the filament is in the opposite direction to the tilting of the
tubulin helices, indicating that the luminal filament most
likely attaches to one tubulin helix at the C3 end and attaches
to the adjacent tubulin helix running underneath at the C6/
C7 end. These attachments suggest that the filament has
intrinsic polarity with two ends making unique contacts
with the C-tubule. The luminal densities in the MT have
been reported previously and presumably stabilize the local
MTstructure (Garvalov et al, 2006; Cyrklaff et al, 2007). The
filamentous structure that we describe in the lumen of the
C-tubule could function as a reinforcement beam to enhance
C-tubule rigidity in the distal half of the basal body.
The emergence of the luminal filaments at the distal half of
the basal body coincides with a structural change at PF C1.
These transitions take place near the middle of the basal
body, about 225nm from the triplet minus (proximal) end
(Figure 4A). The two structures also overlap spatially as the
hook-shaped arm runs across PFs C1 to C4 and the luminal
filament spans PF C3 and PF C6/C7. It is conceivable that
they might interact directly to participate in coordinated
assembly of the basal body C-tubule.
Building a basal body model
Most basal bodies and centrioles are composed of nine
triplets interconnected circumferentially to make a barrel-
shaped structure. In order to find out how the triplets are
linked, we reconstructed the entire basal body based on the
averaged triplet structure. Since the basal bodies were visua-
lized in their near-native state and subvolumes containing
triplet segments were computationally extracted from the
tomogram for alignment and averaging, their spatial coordi-
nates in the context of the entire basal body volume are
known. By using the known subvolume coordinates, we
replaced the subvolumes in each basal body with the aver-
aged triplet structures (as shown in Figure 4B) and recon-
structed entire longitudinal segments of the basal body
without imposing nine-fold symmetry. The results as shown
in Figure 5A and B represent the basal body proximal and
distal ends, respectively. To our surprise, a comparison of the
two ends reveals that the inter-triplet linkages are signifi-
cantly different (black arrows in the right panel of Figure 5A
and B, respectively). At the proximal end, a pointed stub-like
density projects from PFA6 and connects to the neighbouring
triplet at the end of the extended tail of the C-tubule. This
inter-triplet linker is about 130A˚long from the base of the
stub to the tip of the extended tail. In contrast, at the distal
end, the A6 stub connects directly to the outside wall of the
neighbouring C-tubule at PFs C7 and C8 with an approximate
length of 170A˚.
To further analyse the change of this inter-triplet linkage,
we measured the angle between two adjacent triplets. As
shown in Figure 5A and B, a nonagon is created by connect-
ing nine triplet centres in the basal body (red lines), in this
case the centres of B-tubule. Meanwhile, a vector (yellow
arrow) can be drawn across PFs A6–B6–C5/C6, indicating
orientation for each triplet. The angle between the triplet
vector and the nearest side of nonagon defines the relative
Figure 3 Link between the A- and B-tubules in the basal body triplet. (A) Two views showing a large Y-shaped structure lying horizontal
between the A- and B-tubules at the luminal side of the basal body. A stack of these structures forms a longitudinal filament assembly. The
model of MT PFs is in blue. A dashed-line box shows a single 8-nm longitudinal repeat unit. The areas that contact the A- and B-tubules are
highlighted in red. (B) The Y-shaped structure viewed from the luminal side of the basal body. The model of MT PFs is in blue. Two
neighbouring armBs join and form a bifurcated structure as indicated with *. (C) A second A- and B-tubule linker connecting PFs A13 and B10
as indicated with an arrow. The 4-nm periodicity is highlighted with red dots.
Electron cryo-tomography of basal body triplet
S Li et al
The EMBO JournalVOL 31|NO 3|2012
&2012 European Molecular Biology Organization


text:
|Publication number
|Publication type
|Application number
|Publication date
|Oct 5, 2006
|Filing date
|Mar 31, 2006
|Priority date
|Apr 5, 2005
|Also published as
|Publication number
|Robert Baugher
|Original Assignee
|Baugher Robert C
|Export Citation
|BiBTeX, EndNote, RefMan
|Patent Citations (6), Referenced by (2), Classifications (22), Legal Events (3)
|External Links: USPTO, USPTO Assignment, Espacenet
In general, the present invention relates to a cutter used to section elongate materials. More particularly, the present invention relates to a cutter having a rotating blade.
The present invention generally relates to a cutter used to cut elongate products into sections. For example, the cutter may be used to cut extruded profiles with or without reinforcement. These materials have proven difficult to cut with existing cutters.
One existing cutter uses a curved blade that cuts through the material in a scythe like manner. This type of blade may be used to cut material as it comes off an extruder in a continuous manner. Unfortunately, the curved blade cutter often distorts the material as it cuts making it difficult to maintain dimensional accuracy. This distortion also may result in a defective cut surface that is scalloped or otherwise irregular. These problems are pronounced when cutting softer materials.
Another existing cutter operates in a lathe-like manner with the material being mounted inside a rotating mandrel. Since the mandrel has a finite length, extruded material must be pre-cut and mounted before additional cuts are made. Consequently, such cutters are not suitable for continuous operation.
The present invention generally provides a cutter for cutting elongate material into sections, the cutter including a blade motor having a blade shaft, a blade mounted on the blade shaft, and an actuator adapted to move the blade along a drive axis into contact with the material to cut the material.
The present invention further provides a cutter for cutting elongate material into sections, the cutter including a motor coupled to a shaft, wherein the motor selectively rotates the shaft, a blade mounted on the shaft and rotatable therewith, a guard enclosing the blade, the guard defining an opening for receiving the material, a guard shutter mounted adjacent the opening and moveable to selectively cover the opening, and an actuator attached to the guard shutter and adapted to move the guard shutter between an open position and a closed position.
The present invention further provides a cutter for sectioning elongated material, the cutter including a shaft rotatably supported by bearings and coupled to a motor, wherein the motor rotates the shaft, an arm supported on the shaft and extending radially outward relative to the shaft, the arm being rotatably fixed to the shaft and rotatable therewith, a blade mounted on the arm and rotatable independently of the arm, and a blade motor coupled to the blade and adapted to rotate the blade.
The present invention further provides a cutter for cutting elongate material into sections, the cutter including a blade motor having a blade shaft; a blade mounted on the blade shaft, wherein the blade motor is adapted to selectively rotate the blade at a selected speed to cut the material; wherein the blade is supported by an actuator adapted to move the blade into contact with the material to cut the material; and a winding assembly including a spool located downstream of the blade, the spool being adapted to gather the material, and a controller adapted to activate the actuator as the spool becomes full, driving the blade to cut the material.
The cutter according to the present invention generally includes a blade that is rotated on its axis by a motor. The blade speed may be controlled according to the type of material that is being cut. As shown, the blade may be circular and is constructed of a suitable material, such as, a metal or ceramic material. Other materials may be used depending on the particular application. In one example, a surgical steel blade was found suitable for cutting through both soft materials and harder materials, including those containing Kevlar™ fibers. Optionally, a lubricant, such as water, soap, or air, may be applied to the blade to facilitate cutting.
A guard may be provided to reduce the likelihood of injury. The guard may include a slotted opening exposing a portion of the blade. The opening may include walls that guide the material into contact with the blade. A guard shutter may be used to limit exposure to the blade by selectively closing the opening when the blade is not cutting material providing further protection against inadvertent cutting. The shutter may be any member that is moveable to block or otherwise limit access to the opening. The shutter's movement may be controlled manually by a switch or trigger, or controlled automatically by a system controller depending upon the application.
In the example shown in
Motor 20 has a drive shaft 21, which may be housed within a sleeve 22. The drive shaft 21 may connect to a gear box 25. In the example shown in
As shown in
Blade 30 attaches to a blade shaft 27 that extends outward from gear box 25 along the blade's axis B. The blade 30 may be attached to blade shaft 27 in any known manner. In the example shown, the blade 30 includes key 31 that fits within a keyway 29 formed on blade shaft 27.
The blade 30, so connected, is rotated by the motor 20 at a selected speed based on the type of material M that is being cut. In the example shown, the blade 30 is circular having generally circular cutting edge 33 at its radial outward extremity. Other blade shapes suitable for rotary cutting may be used.
As discussed more completely below, the cutter 10 may carry a sensor in monitoring its operation. For example, a sensor 35 may be mounted is sensing relation to the blade 30 to monitor its operation. As will be appreciated, the sensor 35 may be used to generate various information including blade speed, number of revolutions, or simply to determine whether the blade 30 is rotating. In the depicted example, sensor 35 is used to visually check for a broken blade. A second sensor may be used in conjunction with sensor 35 to reduce the likelihood that a broken blade 30 would go undetected. To that end, the second sensor may be circumferentially spaced from sensor 35. In
As best shown in
An opening, generally indicated by the numeral 46, is formed in the guard 40 to expose a portion of the blade 30. While only the edge 33 of blade 30 may be exposed as by an opening in sidewall 44, opening 46 may extend radially inward to allow inward movement of material M relative to blade 30, as shown in
For improved safety, a guard shutter 50 may be provided to selectively close the opening 46. In the example shown, guard shutter 50 is rotatably mounted on guard 40 and may be rotated from a closed position (
To accommodate sensors 35 that protrude inwardly from guard 40, guard shutter 50 may define a slot 51 that extends circumferentially a distance suitable for providing the necessary range of motion for the guard shutter 50 to rotate between the open position (
In accordance with the concepts of the present invention, cutter 10 may be used in connection with a winding assembly, generally indicated by the number 75 in
It will be appreciated that the cut of material M gathered on spool 77 may be timed or a controller C in communication with spool 77 and actuator 79 may be used to detect a selected amount of material on the spool 77 and activate actuator 79 to make a cut. It will be appreciated that the selected amount of material M on spool 77 might not always coincide with the capacity of the spool 77. For sake of simplicity, however, this condition will generally be referred to as the spool being "full."
In the example shown, two spools 77 are mounted on a turret. In this way, once the first spool 77 is full it is rotated by the turret counterclockwise away from the cutter 10 to a cut/unload position 77A. At the same time, an empty spool rotated to a load position 77B adjacent to the cutter 10. In this position, the material M spans both spools 77 and the traverse guide 85 positions the material M in the path of the open gripper 83B on the empty spool. Then, in preparation for the cut, gripper 83B on empty spool grips material M just to the right of the cutter 10. At the time of the cut, the spool 77A stops winding and the gripper 83A on the full spool closes. To make the cut, as actuator 79 drives blade 30 toward material M, the motor brings the blade 30 up to speed and the guard shutter is opened so that the material M is received within the slot formed in the guard as the blade 30 cuts through material M. Once the cut is made, actuator 79 retracts the blade 30 and the guard shutter is closed. Controller C monitors the cutter to ensure that it is in a fully cleared position before spool rotation begins.
Meanwhile, after the cut, the operator may open the gripper 83A on the full spool 77 and removes full spool 77A from the turret. Then, an empty spool is placed on the spindle at the cut/unload position 77A. The process of turreting the spools 77 from the unload position 77A to the load position 77B continues making for a fully automatic winding and cutting system.
An alternate cutter according to the concepts of the present invention is shown in
As shown, the blade pulley 116 and blade 130 may be mounted on opposite sides of the arm 111 with a shaft 119 connecting the blade 130 to the pulley 115. Blade shaft 119 may be supported in suitable bearings, as shown.
The blade 130 may be attached to blade shaft 119 in any known manner including the clamp assembly, generally indicated by the numeral 136 as shown. Clamp assembly 136 is keyed to blade shaft 119 such that it rotates therewith, and includes a chuck 136A on which the blade 130 is mounted. A portion of the chuck 136A extends through blade 130 and has a threaded end onto which a cap assembly 136B is attached to clamp the blade 130 in place. So clamped, blade motor 120 via the belts and pulleys causes the blade 130 to rotate independently of the arm 111.
As best shown in
The speed of arm 111 may also be varied along its rotational path. For example the speed after a cut is made may be increased to bring the blade 130 to the cutting position in a shorter period of time and then slowed to the cut speed at the time of making the cut. In this way, more cuts may be made than when operating the arm 111 at a constant rotational speed. Also, an increase or decrease in the non-cut speed can be used to compensate for the change in speed caused by blade 130 cutting through material M, referred to as "cut dwell." The speeds and cut dwell may be measured in milliseconds (ms). For example, as schematically shown in
One example cut cycle is described in
The example further provides one cut cycle using the given example and discusses the coordination of the cutter 110 and the feeder (not shown). As described in the example, the part is selectively clamped and released as it is cut and then pulled away from the cutter 110 after the cut has been made. To that end, a guiding system may be provided for the exact placement of material. One guiding system includes a pair of arbors 148 split at the point of circular blade travel to support the product during the cutting process. The feeder may move material M at a speed and distance that is timed to provide the required cut length. As described, controller C may use a run/stop motion of the feeder and/or the arm 111 to achieve the desired cut length. As mentioned, the swing arm 111 can have varying speeds that may be independent of the cut window area. In this way, the cutter 110 can provide best cut quality at fast cut per minute rates for short parts, or for a long part, the arm 111 can be stopped until the required length is reached.
A counter weight CW may be attached to the arm 111 on the opposite side of blade 130. The amount of weight and radial position may be adjusted to counterbalance the blade 130.
The cutter 110 may be housed within a shroud to help protect the user and prevent foreign objects from interfering with the cutter's operation.
In another embodiment of the present invention, the cutter is incorporated in a hand-held device. For example, as shown in
The cutter 210 may be provided with a guard 240 that generally surrounds the blade except for an opening 246 exposing a portion of the blade 230. As in the previous embodiment, guard 240 may include a cover 245 attached on one side of the guard 240. The cover may have walls 246 a, 246 b that define an elongated slot-like opening 246 for receiving material M. In the example shown, the opening 246 is formed opposite the handle 275.
As in the previous embodiment, guard shutter 250 may be provided to further protect the user from blade 230 and also to guide the material M into contact with blade 230. In the example shown in
It will be appreciated that other guard shutters may be used including one similar to the shutter 50 described in the first embodiment in connection with cutter 210.
As can be seen from the above description, a novel cutter system has been shown and described. In accordance with the patent statutes, at least one embodiment of the present invention has been described. The embodiments discussed are for example purposes and do not limit the scope of the invention. For an appreciation of the scope of this invention, reference should be made to the appended claims.
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|Feb 25, 2010
|Wenger Manufacturing, Inc.
|Extruder cut-off knife assembly having remote adjustment mechanism
|U.S. Classification
|International Classification
|Cooperative Classification
|European Classification
|Aug 2, 2013
|Maintenance fee reminder mailed
|Dec 19, 2013
|Fee payment
Year of fee payment: 4
|Dec 19, 2013
|Surcharge for late payment